Abstract
Simian virus 40 large T antigen from lytically infected cells has been purified to near homogeneity by immunochromatography of the cell extract on a protein A-Sepharose-monoclonal antibody column. The resulting T antigen retains biochemical activity; i.e., it hydrolyzes ATP and binds to simian virus 40 DNA at the origin of replication.
MeSH Terms
Animals
Antibodies, Monoclonal/immunology
Antigens, Polyomavirus Transforming
Antigens, Viral, Tumor/immunology,isolation & purification
Chromatography, Affinity
Haplorhini
Simian virus 40/immunology
Viral Proteins/immunology,isolation & purification
Chemicals
Antibodies, Monoclonal
Antigens, Polyomavirus Transforming
Antigens, Viral, Tumor
Viral Proteins
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Dixon R A
Nathans D
References (10)
10 references, click to expand
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